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Extraction of Mucin from Rodent Feces and Determination of O-Linked Oligosaccharide Chain Equivalent Derived from Fecal Mucin

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Mucins

Part of the book series: Methods in Molecular Biology ((MIMB,volume 2763))

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Abstract

Since the core protein of mucin in the digesta of the stomach and small intestine, which is less affected by bacteria, remains intact, mucin content can be measured by enzyme-linked immunosorbent assay (ELISA). However, the mucin core protein in bacteria-rich colon digesta and feces is partially hydrolyzed by bacterial enzymes and not fully recognized by mucin antibodies, so mucin cannot be accurately quantified by ELISA. This method quantifies the glycan content linked to the mucin core protein and expresses mucin content in the colon digesta and feces as the equivalent of O-linked oligosaccharide chain. Although mucin glycans are also hydrolyzed by colonic bacteria, this method is a more accurate and simple way to measure mucin content in the digesta of the large intestine and feces than the ELISA method.

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Correspondence to Naomichi Nishimura .

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© 2024 The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature

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Nishimura, N., Tanabe, H., Morita, T. (2024). Extraction of Mucin from Rodent Feces and Determination of O-Linked Oligosaccharide Chain Equivalent Derived from Fecal Mucin. In: Kameyama, A. (eds) Mucins. Methods in Molecular Biology, vol 2763. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-3670-1_2

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  • DOI: https://doi.org/10.1007/978-1-0716-3670-1_2

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  • Publisher Name: Humana, New York, NY

  • Print ISBN: 978-1-0716-3669-5

  • Online ISBN: 978-1-0716-3670-1

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